Cited by 181DNA Repair MechanismsFungal and yeast genetics researchDNA and Nucleic Acid Chemistry

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Fidelity and Processivity of Saccharomyces cerevisiae DNA Polymerase η

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Washington, M. Todd, Johnson, Robert E., Prakash, Satya, Prakash, Louise·1999·Journal of Biological Chemistry

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Abstract

The yeast RAD30 gene functions in error-free replication of UV-damaged DNA, and RAD30 encodes a DNA polymerase, pol eta, that has the ability to efficiently and correctly replicate past a cis-syn-thymine-thymine dimer in template DNA. To better understand the role of pol eta in damage bypass, we examined its fidelity and processivity on nondamaged DNA templates. Steady-state kinetic analyses of deoxynucleotide incorporation indicate that pol eta has a low fidelity, misincorporating deoxynucleotides with a frequency of about 10(-2) to 10(-3). Also pol eta has a low processivity, incorporating only a few nucleotides before dissociating. We suggest that pol eta's low fidelity reflects a flexibility in its active site rendering it more tolerant of DNA damage, while its low processivity limits its activity to reduce errors.

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Enzyme structure and mechanism
Fersht, A. (1977) · Medical Entomology and Zoology · Cited by 2,875
Enzyme structure and mechanism
Elmore, D. T. (1978) · Endeavour · doi:10.1016/0160-9327(78)90081-9 · Cited by 2,713
The XPV (xeroderma pigmentosum variant) gene encodes human DNA polymerase η
Masutani, C., Kusumoto, R., Yamada, A., Dohmae, N., Yokoi, M., Yuasa, M., Araki, M., Iwai, S., Takio, K., & Hanaoka, F. (1999) · Nature · doi:10.1038/21447 · Cited by 1,292
DNA Polymerases: Structural Diversity and Common Mechanisms
Steitz, T. A. (1999) · Journal of Biological Chemistry · doi:10.1074/jbc.274.25.17395 · Cited by 848
Efficient Bypass of a Thymine-Thymine Dimer by Yeast DNA Polymerase, Polη
Johnson, R. E., Prakash, S., & Prakash, L. (1999) · Science · doi:10.1126/science.283.5404.1001 · Cited by 736
Self-citation
hRAD30 Mutations in the Variant Form of Xeroderma Pigmentosum
Johnson, R. E., Kondratick, C. M., Prakash, S., & Prakash, L. (1999) · Science · doi:10.1126/science.285.5425.263 · Cited by 732
Self-citation
FIDELITY MECHANISMS IN DNA REPLICATION
Echols, H., & Goodman, M. F. (1991) · Annual Review of Biochemistry · doi:10.1146/annurev.bi.60.070191.002401 · Cited by 712
Biochemical Basis of DNA Replication Fidelity
Goodman, M. F., Creighton, S., Bloom, L. B., Petruska, J., & Kunkel, T. A. (1993) · Critical Reviews in Biochemistry and Molecular Biology · doi:10.3109/10409239309086792 · Cited by 446
The Saccharomyces cerevisiae RAD30 Gene, a Homologue of Escherichia coli dinB and umuC, Is DNA Damage Inducible and Functions in a Novel Error-Free Postreplication Repair Mechanism
McDonald, J. P., Levine, A. S., & Woodgate, R. (1997) · Genetics · doi:10.1093/genetics/147.4.1557 · Cited by 314
Yeast DNA Repair Proteins Rad6 and Rad18 Form a Heterodimer That Has Ubiquitin Conjugating, DNA Binding, and ATP Hydrolytic Activities
Bailly, V., Lauder, S., Prakash, S., & Prakash, L. (1997) · Journal of Biological Chemistry · doi:10.1074/jbc.272.37.23360 · Cited by 292
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Show all 26 references

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Wang, 1993, Mol. Cell. Biol., 13, 4276

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“This is consistent with several published reports of pol η and other Y-family polymerase activity [6, 12, 15, 60, 61].”
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McCulloch, S. D., Wood, A., Garg, P., Burgers, P., & Kunkel, T. A. (2007) · Biochemistry · doi:10.1021/bi700234t · Cited by 23
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Weil, J.-C., Bertocci, B., Faili, A., Aoufouchi, S., Frey, S., Smet, A. D., Storck, S., Dahan, A., Delbos, F., Weller, S., et al. (2002) · Advances in immunology · doi:10.1016/s0065-2776(02)80015-3 · Cited by 20
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Background
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Background
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InfluentialSelf-citation
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Background
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“(27) did not directly report 4594 Biochemistry, Vol.”
BackgroundResult
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“Calculations were performed as described before.(25,26) The percentage of active NGT was calculated using the following formula:”
BackgroundMethod
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Background
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Masuda, Y., Hanaoka, F., & Masutani, C. (2016) · Springer eBooks · doi:10.1007/978-4-431-55873-6_11 · Cited by 3
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Wang, Z. (2005) · doi:10.1201/9780849352683-32 · Cited by 3
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Self-citation
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Wenson, L., Heldin, J., Martin, M., Erbilgin, Y., Salman, B., Sundqvist, A., Schaal, W., Sandbaumhüter, F. A., Jansson, E. T., Chen, X., et al. (2025) · Nature Communications · doi:10.1038/s41467-025-62512-4 · Cited by 1
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Gening, L. V., Kamensky, A. A., Levitskaya, N. G., Petrochenkov, A. N., Полетаева, И. И., & Tarantul, V. Z. (2005) · Biochemistry (Moscow) · doi:10.1007/s10541-005-0240-y · Cited by 1
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“before dissociating from the DNA template [76].”
Background
Defining error-free postreplication repair in Saccharomyces cerevisiae
Broomfield, S. (2000) · Library and Archives Canada (Government of Canada) · Cited by 1
Saccharomyces cerevisiae DNA helicases Mph1, Srs2 and Sgs1 collaborate for the reinitiation of stalled or collapsed replication forks
Panico, E. R. (2006) · doi:10.53846/goediss-148
DNA Repair in Yeast
Friedberg, E. C., & Fischhaber, P. L. (2006) · Wiley-VCH eBooks · doi:10.1002/3527600906.mcb.200300112
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Substrate recognition by the yeast Rev1 protein and DNA polymerase ζ
Howell, C. A. (2008) · doi:10.17077/etd.fy291k5g
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Tan, T. (2005) · EUR Research Repository (Erasmus University Rotterdam)
Synthetically Lethal Interactions Classify Novel Genes in Postreplication Repair in Saccharomyces cerevisiae
Barbour, L. (2005) · University Library - University of Saskatchewan (University of Saskatchewan)
Effec t of DNA Base Modific ation on Polymerase Chain Reaction Effic iency and Fidelity
Sikorsky, J. A. (2005)
Methods of genetic diversity creation and functional display for directed evolution experiments
Huovinen, T. (2014) · UTUPub (University of Turku)
Role of non-classical polymerases and SUMO PCNA dependent mechanisms in the maintenance of genome stability
Gali, H. (2012) · doi:10.14232/phd.1427
DNA Polymerase Zeta-Dependent Mutagenesis: Molecular Specificity, Extent of Error-Prone Synthesis, and the Role of dNTP Pools
Kochenova, O. V. (2016) · DigitalCommons@UNMC
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Hall, A. (2005) · Journal of International Crisis and Risk Communication Research
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Wang, Z. (2005) · CRC Press eBooks · doi:10.1201/9780849352683.ch24
Caractérisation fonctionnelle de la tolérance aux endommagements de l’ADN des embryons précoces
Furno, E. L. (2019) · theses.fr (ABES) · doi:10.70675/cf32bcd5z3031z4693z8b1bz62fe76673ccc
Insights into the functional coordination of LigD and Ku in bacterial nonhomologous end joining
del Prado, A., Buitrago, A., de Rus-Moreno, A., Bienkowska, I. O., de Ory, A., Díaz-Arco, S., & de Vega, M. (2026) · Scientific Reports · doi:10.1038/s41598-026-47294-z
“…activated DNA as a trap intended to capture LigD Bs molecules that might dissociate during any step of the end-joining reaction, thereby preventing their re-association with the substrate (a methodology previously described for measuring, among others, the processivity of DNA polymerases 32,33 ).”
DNA Polymerase α has Cyclobutane Pyrimidine Dimer Translesion Activity that is Suppressed During Normal Replication
Mukherjee, P., Sarker, A., & Schauer, G. D. (2026) · Journal of Molecular Biology · doi:10.1016/j.jmb.2026.170029
Studies of the Rev1 protein and its role in the replication of damaged DNA
Pryor, J. M. (2012) · doi:10.17077/etd.tvfw78ut
“For example, Pol η is at least 100 fold less accurate and 10 fold less efficient than the replicative DNA polymerase delta when carrying out DNA synthesis on non-damaged substrates [211-213].”
Background

Authors: Washington, M. T., Johnson, R. E., Prakash, S., & Prakash, L.
Affiliations: The University of Texas Medical Branch at Galveston (US)
Corresponding author: Prakash, Louise
ORCID: Washington, M. Todd
Johnson, Robert E.
Prakash, Satya
Prakash, Louise
Venue: Journal of Biological Chemistry
Publisher: Elsevier BV
Published: 1999-12
Volume: 274
Issue: 52
Pages: 36835-36838
ISSN: 0021-9258 (ISSN-L)
DOI: 10.1074/jbc.274.52.36835
OpenAlex: W2107896468
Cited by: 181
References: 26
Citations by year: 2026: 2 · 2025: 2 · 2023: 2 · 2021: 4 · 2020: 3 · 2019: 1 · 2018: 1 · 2017: 4 · 2016: 4 · 2015: 1 · 2014: 5 · 2013: 6 · 2012: 8
FWCI: 6.50
Type: journal article
Language: en
Open access: hybrid
doi.org
Licence: cc-by
www.elsevier.com/tdm/userlicense/1.0/ (tdm)
creativecommons.org/licenses/by/4.0/ (vor, 7617 d)
Locations: Journal of Biological Chemistry (publishedVersion, cc-by)
PubMed (publishedVersion)
Funders: National Institutes of Health (5r01gm019261-30)
National Institute of General Medical Sciences (GM-19261)
Topics: Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › DNA Repair Mechanisms
Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Fungal and yeast genetics research
Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › DNA and Nucleic Acid Chemistry
Keywords: DNA polymerase eta, UV-damaged DNA, translesion synthesis, polymerase fidelity, polymerase processivity, active site flexibility, Saccharomyces cerevisiae
MeSH terms: DNA Polymerase iota, Y-Family DNA Polymerases, DNA Damage, DNA-Directed DNA Polymerase, DNA Replication, Kinetics, Mutation, Saccharomyces cerevisiae

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Fidelity and Processivity of Saccharomyces cerevisiae DNA Polymerase η

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